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. 1991 Feb;11(1):105–118. doi: 10.1007/BF00712803

Comparative studies on the primary structure of acetylcholinesterases from bovine caudate nucleus and bovine erythrocytes

H Heider 1, P Litynski 1, S Stieger 1, U Brodbeck 1,✉
PMCID: PMC11567223  PMID: 2013055

Abstract

  1. Comparison of partial amino acid sequences of G2-acetylcholinesterase (AChE) from bovine erythrocytes and G4-AChE from bovine caudate nucleus revealed no differences in primary structure between the two enyzmes. The first 33 residues of the N-terminal sequences were identical.

  2. In addition, the amino acid sequences of four peptides generated by tryptic and cyanogen bromide cleavage were identical for bovine erthyrocyte and brain AChE, suggesting one identical major coding exon for the adult bovine AChE forms. Comparison of these sequences with that of fetal bovine serum AChE (Doctoret al., 1988), showed differences in residues 16, 181, 212, and 216.

  3. Deglycosylation studies of the two adult enzyme forms revealed that the core protein of erythrocyte AChE has an approximately 4 kDa lower molecular mass than brain AChE. This most propably reflects differences in the C-terminal sequences of the two enzymes.

Key words: acetylcholinesterase, amino acid sequence, amino acid analysis, bovine brain, bovine erythrocytes

Abbreviations

AChE

acetylcholinesterase

BChE

butyrylcholinesterase

PI

phosphatidylinositol

GPI

glycosyl-phosphatidylinositol

SDS-PAGE

sodium dodecyl sulfate-polyacrylamide gel electrophoresis

[3H]DFP

[3H]diisopropylfluorophosphate

PVDF

polyvinylidene difluoride

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